@misc{21284, abstract = {The advantageous characteristics attributed to the 19F nucleus have made it a popular target for NMR once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle-spinning NMR to fluorine-labeled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilized to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR often suffers from slow longitudinal T1 relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton T1 relaxation times, to 19F-labeled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labeled protein via 19F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of 19F MAS NMR experiments without compromising resolution. Additionally, we report the chemical-shift assignments of all four fluorotryptophan signals in the 12 × 39 kDa large protein using a mutagenesis approach.}, author = {Becker, Lea Marie and Schanda, Paul}, publisher = {Institute of Science and Technology Austria}, title = {{Research data for "Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants"}}, doi = {10.15479/AT-ISTA-21284}, year = {2026}, } @article{21929, abstract = {The import of proteins into mitochondria poses fundamental mechanistic challenges: aggregation-prone precursor proteins must be maintained in aqueous compartments and threaded through narrow pores without becoming stuck or mislocalized. Recent evidence from mitochondrial protein import studies and other chaperone systems underscores the critical role of dynamics in balancing sufficiently tight binding, promiscuity, specificity, and release. Dynamic binding of client precursor proteins to import machinery components arises naturally from the avidity of their interactions. Conformational entropy enhances their stability, while the multivalent nature of these interactions ensures that client transfer to downstream insertases occurs without a substantial energy barrier. Here, we discuss this emerging paradigm of dynamic protein handling, using examples where dynamic structures have been resolved and highlight outstanding questions.}, author = {Schneider, Jakob and Guillerm, Undina and Simoes Pereira, Caroline and Schanda, Paul}, issn = {1469-896X}, journal = {Protein Science}, number = {6}, publisher = {Wiley}, title = {{Dynamic disorder is crucial for mitochondrial protein import}}, doi = {10.1002/pro.70630}, volume = {35}, year = {2026}, } @article{21777, abstract = {The advantageous characteristics attributed to the 19F nucleus have made it a popular target for nuclear magnetic resonance (NMR) once again in recent years. Aside from solution NMR, an increasing number of studies have been conducted applying solid-state magic-angle spinning (MAS) NMR to fluorine-labelled samples. Here, the high chemical shift anisotropy and strong dipolar couplings can be utilised to get structural insights into proteins and measure long distances. Despite increasing popularity and promising benefits, the sensitivity of biomolecular 19F MAS NMR often suffers from slow longitudinal T1 relaxation and therefore long recycle delays. In this work, we expand paramagnetic doping, an approach commonly used to reduce proton T1 relaxation times, to 19F-labelled biological samples. We study the effect of Gd(DTPA) and Gd(DTPA-BMA) on 19F T1 and T2, and 13C T1 and T2 relaxation in a [5-19F13C]-tryptophan-labelled protein via 19F-detected MAS NMR experiments. The observed paramagnetic relaxation enhancement substantially reduces measurement times of 19F MAS NMR experiments without compromising resolution. Additionally, we report the chemical shift assignments of all four fluorotryptophan signals in the 12×39 kDa-large protein TET2 using a mutagenesis approach.}, author = {Becker, Lea Marie and Toscano, Giorgia and Kapitonova, Anna and Singh, Rajkumar and Guillerm, Undina and Lichtenecker, Roman J. and Schanda, Paul}, issn = {2699-0016}, journal = {Magnetic Resonance}, number = {1}, pages = {29--37}, publisher = {Copernicus Publications}, title = {{Accelerated 19F biomolecular magic-angle spinning NMR with paramagnetic dopants}}, doi = {10.5194/mr-7-29-2026}, volume = {7}, year = {2026}, } @article{22638, abstract = {The one-bond proton-carbon coupling constant (1JCH) is an insightful probe of carbohydrate configuration. Equatorial and axial protons at the C1 position typically exhibit distinct 1JCH values, enabling NMR measurements to distinguish α- and β-configurations in carbohydrates. In principle, such measurements could provide insights into carbohydrates in the cell walls of intact microbes. However, traditionally, these measurements are performed by solution NMR with carbohydrates that were extracted, solubilized and fractionated, leaving the biological relevance of the measurements uncertain. Here, we demonstrate that 1H-detected solid-state NMR with fast magic-angle spinning allows quantitative measurements of 1JCH couplings for mobile capsular polysaccharides, directly on submilligram amounts of pathogenic cells. Our approach is demonstrated on intact cells of the pathogenic yeast Cryptococcus neoformans. High-resolution proton-detected spectra enabled the determination of coupling constants for five mobile polysaccharide units of the cryptococcal capsule, revealing their native configurations and confirming previous solution NMR-based anomeric configuration assignments.}, author = {Lends, Alons and Lamon, Gaelle and Vallet, Alicia and Grélard, Axelle and Morvan, Estelle and Aimanianda, Vishukumar and Schanda, Paul and Loquet, Antoine}, issn = {1520-5126}, journal = {Journal of the American Chemical Society}, number = {27}, pages = {28037--28042}, publisher = {American Chemical Society}, title = {{On-cell detection of polysaccharide one-bond1Jch couplings by proton-detected solid-state NMR}}, doi = {10.1021/jacs.6c06064}, volume = {148}, year = {2026}, } @article{22268, abstract = {AlphaFold3 predicts highly accurate protein structures from sequence but tends to collapse to a single dominant conformation, even when the underlying structure is inherently heterogeneous. Moreover, its predictions are oblivious to experimental conditions that can alter local sequence conformation. In this work, we show that AlphaFold3 can be guided to match data obtained by nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography and cryogenic electron microscopy (cryo-EM) experiments and combinations thereof. Our approach can also incorporate data that explicitly report on dynamics, such as site-resolved order parameters. We demonstrate that this methodology generates compact structural ensembles whose ensemble-averaged observables agree with experiment, with fewer distance restraint violations than traditionally resolved NMR structures and with unmodeled alternate conformations uncovered in electron density. This methodology paves the way for experimentally aware predictive models that generate structural ensembles consistent with the measurements, potentially over multiple modalities, and that can be further refined toward thermodynamically grounded ensembles by incorporating energetics.}, author = {Maddipatla, Sai A and Sellam, Nadav E and Bojan, Meital I and Masalitin, Vova and Vedula, Sanketh and Schanda, Paul and Marx, Ailie and Bronstein, Alexander}, issn = {1546-1696}, journal = {Nature Biotechnology}, publisher = {Springer Nature}, title = {{Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles}}, doi = {10.1038/s41587-026-03166-5}, year = {2026}, } @phdthesis{22334, abstract = {Characterizing protein dynamics at the atomic level is essential for our understanding of biological mechanisms. Whether it is to facilitate metabolite transport, catalyze reactions, transmit signals, or regulate metabolism – proteins are constantly in motion and sample multiple conformational states to fulfill their function. Nuclear magnetic resonance (NMR) spectroscopy is particularly well suited to elucidate the dynamics of biomolecules on their complex free-energy landscape. In particular, solid-state magic-angle spinning (MAS) NMR enables the study of large molecular assemblies, protein crystals, or insoluble proteins at atomic resolution without an inherent molecular size limitation. MAS NMR experiments to probe protein dynamics are extremely versatile and sensitive to motional timescales from picoseconds to seconds. Over the past decades, technological advances, developments in experimental design, and new isotope-labeling approaches have further expanded the possibilities of this technique and significantly improved the accuracy of the determined motional parameters. Functionally important sites of proteins often contain aromatic residues. Their side-chain motions have therefore long served as valuable indicators of mechanistically relevant dynamics in NMR studies. In this thesis, site-specifically labeled aromatic residues act as sensitive reporters for MAS NMR studies of protein dynamics. The first part addresses how different environments impact side-chain motion by probing ring flips of phenylalanines and tyrosines in crystalline proteins and amyloid fibrils. It provides important insights for the analysis of dynamics obtained in non-native protein environments and emphasizes the complex factors that determine the timescale of internal dynamics. In the second part, the focus shifts towards methodological questions regarding the investigation of protein dynamics by 19F MAS NMR. The fluorine nucleus exhibits promising characteristics for NMR studies but also presents significant challenges, which is why the full methodological potential of 19F MAS NMR has not been fully realized yet. This work demonstrates that paramagnetic doping can considerably reduce the measurement time and improve the sensitivity of fluorinated samples. Finally, 19F MAS NMR is evaluated as a tool for studying protein side-chain dynamics on the example of tryptophans. The results illustrate the challenges in analyzing such experiments and lay the foundation for further development of 19F MAS NMR relaxation studies. Taken together, this thesis highlights the potential of combining specific isotope labeling, MAS NMR, and complementary methods such as crystallography and computational simulations to elucidate internal protein dynamics. The further development of such integrative approaches will be crucial to improving our understanding of complex mechanisms and protein function. }, author = {Becker, Lea Marie}, isbn = {978-3-99078-084-8}, issn = {2663-337X}, pages = {205}, publisher = {Institute of Science and Technology Austria}, title = {{Exploring protein dynamics using specific labeling approaches for solid-state MAS NMR}}, doi = {10.15479/AT-ISTA-22334}, year = {2026}, } @article{22105, abstract = {Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein–protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labelling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a crystal structure of a GB1 variant reported in this work, reproduce these elevated barriers and reveal how the crystal restrains motions.}, author = {Becker, Lea Marie and Fu, Haohao and Tatman, Benjamin and Dreydoppel, Matthias and Kapitonova, Anna and Balazs, Daniel and Weininger, Ulrich and Engilberge, Sylvain and Chipot, Christophe and Schanda, Paul}, issn = {17554349}, journal = {Nature Chemistry}, pages = {1221--1230}, publisher = {Springer Nature}, title = {{Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes}}, doi = {10.1038/s41557-026-02155-0}, volume = {18}, year = {2026}, } @misc{21145, abstract = {Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. }, author = {Becker, Lea Marie and Schanda, Paul and Chipot, Christophe}, publisher = {Institute of Science and Technology Austria}, title = {{Additional Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes"}}, doi = {10.15479/AT-ISTA-21145}, year = {2026}, } @inproceedings{22722, abstract = {The local structure of a protein strongly impacts its function and interactions with other molecules. Representing local biomolecular environments remains a key challenge while applying machine learning approaches over protein structures. The structural and chemical variability of these environments makes them challenging to model, and performing representation learning on these objects remains largely under-explored. In this work, we propose representations for local protein environments that leverage intermediate features from machine learning force fields (MLFFs). We extensively benchmark state-of-the-art MLFFs, comparing their performance across latent spaces and downstream tasks, and show that their embeddings capture local structural (e.g., secondary motifs) and chemical features (e.g., amino acid identity and protonation state), organizing protein environments into a structured manifold. We show that these representations enable zero-shot generalization and transfer across diverse downstream tasks. As a case study, we build a physics-informed, uncertainty-aware chemical shift predictor that achieves state-of-the-art accuracy in biomolecular NMR spectroscopy. Our results establish MLFFs as general-purpose, reusable representation learners for protein modeling, opening new directions in representation learning for structured physical systems. Code and data are available at https://github.com/mb012/MLFF_representation. }, author = {Bojan, Meital I and Vedula, Sanketh and Maddipatla, Sai A and Sellam, Nadav E and Rzayev, Anar and Napoli, Federico and Schanda, Paul and Bronstein, Alexander}, booktitle = {14th International Conference on Learning Representations}, location = {Rio de Janeiro, Brazil}, pages = {100760--100799}, title = {{Representing local protein environments with machine learning force fields}}, volume = {2026}, year = {2026}, } @misc{22687, abstract = {Understanding enzyme function requires characterizing not only static structure but also dynamics and ligand interactions. NMR spectroscopy provides this insight at atomic resolution, yet for large proteins the difficulty of resonance assignment has largely confined such studies to systems below ∼50 kDa, or to observing only methyl groups. Here we present an integrated magic-angle spinning (MAS) and solution NMR study of the 134 kDa tetrameric malate dehydrogenase from Ignicoccus islandicus (IiMDH), an enzyme of particular interest as an evolutionary intermediate between allosteric lactate dehydrogenases and non-allosteric malate dehydrogenases. By combining high-dimensional (up to 4D) MAS NMR experiments on sedimented protein with solution NMR, we achieved 92% backbone heavy- atom assignment and 91% assignment of all Ile-δ1, Leu-δ1/-δ2, Val-γ1/-γ2, Met-ε and Thr-γ methyl groups. Building on these assignments, we use various probes of backbone and sidechain dynamics: elevated MAS NMR 15N rotating-frame relaxation (R1ρ) points to microsecond motions in functionally critical regions, including the catalytic loop and the mobile surface loop. Complementary methyl-axis order parameters from solution NMR identified additional flexible sites in the hydrophobic core. Chemical shift perturbation experiments upon addition of the substrate analogue oxamate, monitored via backbone 1H-15N TROSY, revealed both active-site contacts and responses in helices α2F and α3G, regions implicated in allosteric signal transmission. The integrated approach demonstrated here exploits the distinct strengths of MAS and solution NMR, and provides a comprehensive view of structure, dynamics, and substrate interactions in a large oligomeric enzyme that would not be accessible by either technique alone.}, author = {Schanda, Paul and Napoli, Federico}, publisher = {Institute of Science and Technology Austria}, title = {{Data and scripts for: "Integrated solid/solution NMR assignment allows mapping dynamics and ligand binding in a 134 kDa enzyme"}}, doi = {10.15479/AT-ISTA-22687}, year = {2026}, } @inproceedings{21327, abstract = {Proteins exist as a dynamic ensemble of multiple conformations, and these motions are often crucial for their functions. However, current structure prediction methods predominantly yield a single conformation, overlooking the conformational heterogeneity revealed by diverse experimental modalities. Here, we present a framework for building experiment-grounded protein structure generative models that infer conformational ensembles consistent with measured experimental data. The key idea is to treat stateof-the-art protein structure predictors (e.g., AlphaFold3) as sequence-conditioned structural priors, and cast ensemble modeling as posterior inference of protein structures given experimental measurements. Through extensive real-data experiments, we demonstrate the generality of our method to incorporate a variety of experimental measurements. In particular, our framework uncovers previously unmodeled conformational heterogeneity from crystallographic densities, and generates high-accuracy NMR ensembles orders of magnitude faster than the status quo. Notably, we demonstrate that our ensembles outperform AlphaFold3 (Abramson et al., 2024) and sometimes better fit experimental data than publicly deposited structures to the Protein Data Bank (PDB, Burley et al. (2017)). We believe that this approach will unlock building predictive models that fully embrace experimentally observed conformational diversity.}, author = {Maddipatla, Sai A and Sellam, Nadav E and Bojan, Meital I and Vedula, Sanketh and Schanda, Paul and Marx, Ailie and Bronstein, Alexander}, booktitle = {Proceedings of the 42nd International Conference on Machine Learning}, issn = {2640-3498}, location = {Vancouver, Canada}, pages = {42366 -- 42393}, publisher = {ML Research Press}, title = {{Inverse problems with experiment-guided AlphaFold}}, volume = {267}, year = {2025}, } @article{19072, abstract = {Pathogenic fungal and bacterial cells are enveloped within a cell wall, a molecular barrier at their cell surface, and a critical architecture that constantly evolves during pathogenesis. Understanding the molecular composition, structural organization, and mobility of polysaccharides constituting this cell envelope is crucial to correlate cell wall organization with its role in pathogenicity and to identify potential antifungal targets. For the fungal pathogen Cryptococcus neoformans, the characterization of the cell envelope has been complexified by the presence of an additional external polysaccharide capsular shell. Here, we investigate how magic-angle spinning (MAS) solid-state NMR techniques increase the analytical capabilities to characterize the structure and dynamics of this encapsulated pathogen. The versatility of proton detection experiments, dynamic-based filters, and relaxation measurements facilitate the discrimination of the highly mobile external capsular structure from the internal rigid cell wall of C. neoformans. In addition, we report the in situ detection of triglyceride molecules from lipid droplets based on NMR dynamic filters. Together, we demonstrate a nondestructive technique to study the cell wall architecture of encapsulated microbes using C. neoformans as a model, an airborne opportunistic fungal pathogen that infects mainly immunocompromised but also competent hosts.}, author = {Lends, Alons and Lamon, Gaelle and Delcourte, Loic and Sturny-Leclere, Aude and Grélard, Axelle and Morvan, Estelle and Abdul-Shukkoor, Muhammed Bilal and Berbon, Mélanie and Vallet, Alicia and Habenstein, Birgit and Dufourc, Erick J. and Schanda, Paul and Aimanianda, Vishukumar and Loquet, Antoine}, issn = {1520-5126}, journal = {Journal of the American Chemical Society}, number = {8}, pages = {6813--6824}, publisher = {American Chemical Society}, title = {{Molecular distinction of cell wall and capsular polysaccharides in encapsulated pathogens by in situ magic-angle spinning NMR techniques}}, doi = {10.1021/jacs.4c16975}, volume = {147}, year = {2025}, } @article{19555, abstract = {The charged arginine side chain is unique in determining many innate properties of proteins, contributing to stability and interaction surfaces, and directing allosteric regulation and enzymatic catalysis. NMR experiments can be used to reveal these processes at the molecular level, but it often requires selective insertion of carbon-13, nitrogen-15, and deuterium at defined atomic positions. We introduce a method to endow arginine residues with defined isotope patterns, combining synthetic organic chemistry and cell-based protein overexpression. The resulting proteins feature NMR active spin systems with optimized relaxation pathways leading to simplified NMR spectra with a sensitive response to changes in the chemical environment of the nuclei observed.}, author = {Rohden, Darja and Toscano, Giorgia and Schanda, Paul and Lichtenecker, Roman J.}, issn = {1521-3765}, journal = {Chemistry - A European Journal}, number = {24}, publisher = {Wiley}, title = {{Synthesis of selectively 13C/2H/15N- labeled arginine to probe protein conformation and interaction by NMR spectroscopy}}, doi = {10.1002/chem.202500408}, volume = {31}, year = {2025}, } @misc{19696, author = {Tatman, Benjamin}, publisher = {Institute of Science and Technology Austria}, title = {{Dataset for "Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State"}}, doi = {10.15479/AT-ISTA-19696}, year = {2025}, } @article{20184, abstract = {Specialized DNA polymerases facilitate various cellular processes. Despite extensive research, the mutagenic effects of these error-prone enzymes on genomes are not fully understood. Here we show that Pol IV promotes genomic instability in Pseudomonas aeruginosa by misincorporating oxidized guanine nucleotides. This activity led to a distinctive mutational signature, characterized by A-to-C transversions occurring preferentially at AT sites flanked by a 5’G and/or 3’C. Furthermore, Pol IV preferentially targeted pathogenicity genes located at specific chromosomal locations near the replication termination region and rRNA-encoding operons. Half of the mutation events catalyzed by Pol IV impaired gene function. This can be attributed to the bias of Pol IV for mutating codons with its preferred sequence contexts, leading to substitutions to unreactive alanine and glycine residues. Remarkably, mutation signatures identified for Pol IV were found in clinical isolate genomes of P. aeruginosa, providing compelling evidence for its role in genetic diversification during pathogen adaptation.}, author = {Castell, Sofía D. and Fernandez, Consuelo M. and Tumas, Ignacio N. and Margara, Lucía M. and Miserendino, Maria C and Ceschin, Danilo G. and Pezza, Roberto J. and Monti, Mariela R.}, issn = {2399-3642}, journal = {Communications Biology}, publisher = {Springer Nature}, title = {{The low-fidelity DNA Pol IV accelerates evolution of pathogenicity genes in Pseudomonas aeruginosa}}, doi = {10.1038/s42003-025-08589-5}, volume = {8}, year = {2025}, } @misc{20242, abstract = {This repository contains calculations of carbon footprints of NMR conferences, as described in the article by Lucky N. Kapoor, Natalia Ruzickova, Predrag Živadinović, Valentin Leitner, Maria Anna Sisak, Cecelia Mweka, Jeroen Dobbelaere, Georgios Katsaros, and Paul Schanda Published in Magnetic Resonance, 2025.}, author = {Schanda, Paul}, keywords = {sustainability, conference travel}, publisher = {Institute of Science and Technology Austria}, title = {{Data of: "Quantifying the carbon footprint of conference travel: the case of NMR meetings"}}, doi = {10.15479/AT-ISTA-20242}, year = {2025}, } @article{20321, abstract = {Microsecond-to-millisecond motions are instrumental for many biomolecular functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique for studying these dynamic processes. While BMRD experiments are routinely used to probe protein motions in solution, the experiment is more demanding in the solid state, where dipolar couplings complicate the spin dynamics. It is believed that high deuteration levels are required and sufficient to obtain accurate and quantitative data. Here we show that even under fast magic-angle spinning and high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common. The origin of these artifacts is identified as a second-order three-spin Mixed Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts are found to be a significant confounding factor for the accurate quantification of microsecond protein dynamics using BMRD in the solid state. We show that the application of low-power continuous wave (CW) decoupling simultaneously with the 15N spin-lock leads to the suppression of these conditions and enables quantitative measurements of microsecond exchange in the solid state. Remarkably, the application of decoupling allows the measurement of accurate BMRD even in fully protonated proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements in MAS NMR.}, author = {Tatman, Benjamin and Sridharan, Vidhyalakshmi and Uttarkabat, Motilal and Jaroniec, Christopher P. and Ernst, Matthias and Rovo, Petra and Schanda, Paul}, issn = {1520-5126}, journal = {Journal of the American Chemical Society}, number = {32}, pages = {29315--29326}, publisher = {American Chemical Society}, title = {{Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR}}, doi = {10.1021/jacs.5c09057}, volume = {147}, year = {2025}, } @article{20664, abstract = {Conference travel contributes to the climate footprint of academic research. Here, we provide a quantitative estimate of the carbon emissions associated with conference attendance by analyzing travel data from participants of 10 international conferences in the field of magnetic resonance, namely EUROMAR, ENC and ICMRBS. We find that attending a EUROMAR conference produces, on average, more than 1 t CO2 eq.. For the analyzed conferences outside Europe, the corresponding value is about 2–3 times higher, on average, with intercontinental trips amounting to up to 5 t. We compare these conference-related emissions to other activities associated with research and show that conference travel is a substantial portion of the total climate footprint of a researcher in magnetic resonance. We explore several strategies to reduce these emissions, including the impact of selecting conference venues more strategically and the possibility of decentralized conferences. Through a detailed comparison of train versus air travel – accounting for both direct and infrastructure-related emissions – we demonstrate that train travel offers considerable carbon savings. These data may provide a basis for strategic choices of future conferences in the field and for individuals deciding on their conference attendance.}, author = {Kapoor, Lucky and Ruzickova, Natalia and Zivadinovic, Predrag and Leitner, Valentin and Sisak, Maria A and Mweka, Cecelia N and Dobbelaere, Jeroen A and Katsaros, Georgios and Schanda, Paul}, issn = {2699-0016}, journal = {Magnetic Resonance}, number = {2}, pages = {243--256}, publisher = {Copernicus Publications}, title = {{Quantifying the carbon footprint of conference travel: The case of NMR meetings}}, doi = {10.5194/mr-6-243-2025}, volume = {6}, year = {2025}, } @misc{20641, abstract = {Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. }, author = {Becker, Lea Marie and Schanda, Paul}, publisher = {Institute of Science and Technology Austria}, title = {{Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes"}}, doi = {10.15479/AT-ISTA-20641}, year = {2025}, } @article{20538, abstract = {In this study, we describe an integrated approach for methyl group assignment comprising precursor-based selective methyl group labeling, a novel pulse sequence for methyl to backbone coherence transfer and chemical shift predictions using UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal methyl groups of leucine and valine residues to each other and to the protein backbone. By additional 13C,2H-labeling of residues other than valine and leucine residues of the protein, important chemical shift information about neighboring residues (following valine and leucine residues) can be achieved. Thus, different valine and leucine residues in a protein can be characterized as a specific chemical shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0 using experimental data taken from a subset of the BMRB database revealed a correct assignment performance of about 90%. With applications to proteins of 60.2 kDa and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides valuable information even for very large proteins.}, author = {Knödlstorfer, Sonja and Toscano, Giorgia and Ptaszek, Aleksandra L. and Kontaxis, Georg and Napoli, Federico and Schneider, Jakob and Maier, Katharina and Kapitonova, Anna and Lichtenecker, Roman J. and Schanda, Paul and Konrat, Robert}, issn = {1089-8638}, journal = {Journal of Molecular Biology}, number = {23}, publisher = {Elsevier}, title = {{A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0}}, doi = {10.1016/j.jmb.2025.169465}, volume = {437}, year = {2025}, }